ATF5 Connects the Pericentriolar Materials to the Proximal End of the Mother Centriole
- Cell. 2015 Jul 30;162(3):580-92. doi: 10.1016/j.cell.2015.06.055.
- 1. Department of Pharmaceutical Sciences, Washington State University College of Pharmacy, Spokane, WA 99202, USA.
- 2. Department of Pharmacology, Penn State College of Medicine, Hershey, PA 17033, USA.
- 3. State Key Laboratory of Cell Biology, Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China; Xinyuan Institute of Medicine and Biotechnology, College of Life Science, Zhejiang Sci-Tech University, Hangzhou 310018, China.
- 4. Brain Tumor Center and Department of Neuro-Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
- 5. Department of Pharmaceutical Sciences, Washington State University College of Pharmacy, Spokane, WA 99202, USA. Electronic address: [email protected].
Although it is known that the centrioles play instructive roles in pericentriolar material (PCM) assembly and that the PCM is essential for proper centriole formation, the mechanism that governs centriole-PCM interaction is poorly understood. Here, we show that ATF5 forms a characteristic 9-fold symmetrical ring structure in the inner layer of the PCM outfitting the proximal end of the mother centriole. ATF5 controls the centriole-PCM interaction in a cell-cycle- and centriole-age-dependent manner. Interaction of ATF5 with polyglutamylated tubulin (PGT) on the mother centriole and with PCNT in the PCM renders ATF5 as a required molecule in mother centriole-directed PCM accumulation and in PCM-dependent centriole formation. ATF5 depletion blocks PCM accumulation at the centrosome and causes fragmentation of centrioles, leading to the formation of multi-polar mitotic spindles and genomic instability. These data show that ATF5 is an essential structural protein that is required for the interaction between the mother centriole and the PCM.